- Glucose transporter
Glucose transporters are a wide group of membrane proteins that facilitate the transport of glucose over a plasma membrane. Because glucose is a vital source of energy for all life these transporters are present in all phyla. The GLUT or SLC2A family are a protein family that is found in most mammalian cells.
Synthesis of free glucose
Most non-autotrophic cells are unable to produce free glucose because they lack expression of glucose-6-phosphatase and, thus, are involved only in glucose uptake and catabolism. Usually only produced in hepatocytes, in fasting conditions other tissues such as the intestines, muscles, brain and kidneys are able to produce glucose following activation of gluconeogenesis.
Glucose transport in yeast
Name Properties Notes Snf3 low-glucose sensor; repressed by glucose; low expression level; repressor of Hxt6 Rgt2 high-glucose sensor; low expression level Hxt1 Km: 100 mM, 129 - 107 mM low-affinity glucose transporter; induced by high glucose level Hxt2 Km = 1.5 - 10 mM high/intermediate-affinityglucose transporter; induced by low glucose level Hxt3 Vm = 18.5, Kd = 0.078, Km = 28.6/34.2 - 60 mM low-affinity glucose transporter Hxt4 Vm = 12.0, Kd = 0.049, Km = 6.2 intermediate-affinity glucose transporter Hxt5 Km = 10 mM Moderate glucose affinity. Abundant during stationary phase, sporulation and low glucose conditions. Transcription repressed by glucose. Hxt6 Vm = 11.4, Kd = 0.029, Km = 0.9/14, 1.5 mM high glucose affinity Hxt7 Vm = 11.7, Kd = 0.039, Km = 1.3, 1.9, 1.5 mM high glucose affinity Hxt8 low expression level Hxt9 involved in pleiotropic drug resistance Hxt11 involved in pleiotropic drug resistance Gal2 Vm = 17.5, Kd = 0.043, Km = 1.5, 1.6 high galactose affinity
Glucose transport in Mammals
GLUTs are integral membrane proteins that contain 12 membrane-spanning helices with both the amino and carboxyl termini exposed on the cytoplasmic side of the plasma membrane. GLUT proteins transport glucose and related hexoses according to a model of alternate conformation, which predicts that the transporter exposes a single substrate binding site toward either the outside or the inside of the cell. Binding of glucose to one site provokes a conformational change associated with transport, and releases glucose to the other side of the membrane. The inner and outer glucose-binding sites are, it seems, located in transmembrane segments 9, 10, 11; also, the QLS motif located in the seventh transmembrane segment could be involved in the selection and affinity of transported substrate.
Each glucose transporter isoform plays a specific role in glucose metabolism determined by its pattern of tissue expression, substrate specificity, transport kinetics, and regulated expression in different physiological conditions. To date, 13 members of the GLUT/SLC2 have been identified. On the basis of sequence similarities, the GLUT family has been divided into three subclasses.
Class I comprises the well-characterized glucose transporters GLUT1-GLUT4.
Name Distribution Notes GLUT1 Is widely distributed in fetal tissues. In the adult, it is expressed at highest levels in erythrocytes and also in the endothelial cells of barrier tissues such as the blood-brain barrier. However, it is responsible for the low-level of basal glucose uptake required to sustain respiration in all cells. Levels in cell membranes are increased by reduced glucose levels and decreased by increased glucose levels. GLUT2 Is a bidirectional transporter, allowing glucose to flow in 2 directions. Is expressed by renal tubular cells, small intestinal epithelial cells, liver cells and pancreatic β cells. Bidirectionality is required in liver cells to uptake glucose for glycolysis, and release of glucose during gluconeogenesis. In pancreatic β-cells, free flowing glucose is required so that the intracellular environment of these cells can accurately gauge the serum glucose levels. All three monosaccharides (glucose, galactose and fructose) are transported from the intestinal mucosal cell into the portal circulation by GLUT2 Is a high-capacity and low-affinity isoform GLUT3 Expressed mostly in neurons (where it is believed to be the main glucose transporter isoform), and in the placenta. Is a high-affinity isoform, allowing it to transport even in times of low glucose concentrations. GLUT4 Found in adipose tissues and striated muscle (skeletal muscle and cardiac muscle). Is the insulin-regulated glucose transporter. Responsible for insulin-regulated glucose storage.
Class II comprises:
- GLUT5 (SLC2A5), a fructose transporter
- GLUT7 - SLC2A7 - (SLC2A7), transporting glucose out of the endoplasmic reticulum 
- GLUT9 - SLC2A9 - (SLC2A9)
- GLUT11 (SLC2A11)
Class III comprises:
- GLUT6 (SLC2A6),
- GLUT8 (SLC2A8),
- GLUT10 (SLC2A10),
- GLUT12 (SLC2A12), and
- the H+/myoinositol transporter HMIT (SLC2A13).
Most members of classes II and III have been identified recently in homology searches of EST databases and the sequence information provided by the various genome projects.
The function of these new glucose transporter isoforms is still not clearly defined at present. Several of them (GLUT6, GLUT8) are made of motifs that help retain them intracellularly and therefore prevent glucose transport. Whether mechanisms exist to promote cell-surface translocation of these transporters is not yet known, but it has clearly been established that insulin does not promote GLUT6 and GLUT8 cell-surface translocation.
Discovery of sodium-glucose cotransport
In August 1960, in Prague, Robert K. Crane presented for the first time his discovery of the sodium-glucose cotransport as the mechanism for intestinal glucose absorption. Crane's discovery of cotransport was the first ever proposal of flux coupling in biology. 
- ^ a b c d e f g h Maier A, Asano T, Volker A, Boles E, Fuhrmann G F (2002). "Characterisation of glucose transport in Saccharomyces cerevisiae with plasma membrane vesicles (countertransport) and intact cells (initial uptake) with single Hxt1, Hxt2, Hxt3, Hxt4, Hxt6, Hxt7 or Gal2 transporters". FEMS Yeast Research 2 (4): 539–550. doi:10.1111/j.1567-1364.2002.tb00121.x. PMID 12702270.
- ^ uniprot list of possible glucose transporters in S. cerevisiae
- ^ a b c d e f g h i j k l m n Boles E, Hollenberg C P (1997). "The molecular genetics of hexose transport in yeasts". FEMS Microbiology Reviews 21 (1): 85–111. doi:10.1111/j.1574-6976.1997.tb00346.x. PMID 9299703.
- ^ a b Diderich J A, Schuurmans J M, Gaalen M C, Kruckeberg A L, Van Dam K (2001). "Functional analysis of the hexose transporter homologue HXT5 in Saccharomyces cerevisiae". Yeast 18 (16): 1515–1524. doi:DOI: 10.1002 / yea.779. PMID 11748728.
- ^ Oka Y, Asano T, Shibasaki Y, Lin J, Tsukuda K, Katagiri H, Akanuma Y, Takaku F (1990). "C-terminal truncated glucose transporter is locked into an inward-facing form without transport activity". Nature 345 (6275): 550–3. doi:10.1038/345550a0. PMID 2348864.
- ^ Hebert D, Carruthers A (1992). "Glucose transporter oligomeric structure determines transporter function. Reversible redox-dependent interconversions of tetrameric and dimeric GLUT1". J. Biol. Chem. 267 (33): 23829–38. PMID 1429721.
- ^ Cloherty E, Sultzman L, Zottola R, Carruthers A (1995). "Net sugar transport is a multistep process. Evidence for cytosolic sugar binding sites in erythrocytes". Biochemistry 34 (47): 15395–406. doi:10.1021/bi00047a002. PMID 7492539.
- ^ Hruz P, Mueckler M (2001). "Structural analysis of the GLUT1 facilitative glucose transporter (review)". Mol. Membr. Biol. 18 (3): 183–93. doi:10.1080/09687680110072140. PMID 11681785.
- ^ Seatter M, De la Rue S, Porter L, Gould G (1998). "QLS motif in transmembrane helix VII of the glucose transporter family interacts with the C-1 position of D-glucose and is involved in substrate selection at the exofacial binding site". Biochemistry 37 (5): 1322–6. doi:10.1021/bi972322u. PMID 9477959.
- ^ Hruz P, Mueckler M (1999). "Cysteine-scanning mutagenesis of transmembrane segment 7 of the GLUT1 glucose transporter". J. Biol. Chem. 274 (51): 36176–80. doi:10.1074/jbc.274.51.36176. PMID 10593902.
- ^ Thorens B (1996). "Glucose transporters in the regulation of intestinal, renal, and liver glucose fluxes". Am. J. Physiol. 270 (4 Pt 1): G541–53. PMID 8928783.
- ^ Joost H, Thorens B (2001). "The extended GLUT-family of sugar/polyol transport facilitators: nomenclature, sequence characteristics, and potential function of its novel members (review)". Mol. Membr. Biol. 18 (4): 247–56. doi:10.1080/09687680110090456. PMID 11780753.
- ^ Bell G, Kayano T, Buse J, Burant C, Takeda J, Lin D, Fukumoto H, Seino S (1990). "Molecular biology of mammalian glucose transporters". Diabetes Care 13 (3): 198–208. doi:10.2337/diacare.13.3.198. PMID 2407475.
- ^ Page 995 in: Walter F., PhD. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. pp. 1300. ISBN 1-4160-2328-3.
- ^ Uldry M, Thorens B (2004). "The SLC2 family of facilitated hexose and polyol transporters". Pflugers Arch. 447 (5): 480–9. doi:10.1007/s00424-003-1085-0. PMID 12750891.
- ^ Robert K. Crane, D. Miller and I. Bihler. “The restrictions on possible mechanisms of intestinal transport of sugars”. In: Membrane Transport and Metabolism. Proceedings of a Symposium held in Prague, August 22–27, 1960. Edited by A. Kleinzeller and A. Kotyk. Czech Academy of Sciences, Prague, 1961, pp. 439-449.
- ^ Ernest M. Wright and Eric Turk. “The sodium glucose cotransport family SLC5”. Pflügers Arch 447, 2004, p. 510. “Crane in 1961 was the first to formulate the cotransport concept to explain active transport . Specifically, he proposed that the accumulation of glucose in the intestinal epithelium across the brush border membrane was [is] coupled to downhill Na+ transport cross the brush border. This hypothesis was rapidly tested, refined, and extended [to] encompass the active transport of a diverse range of molecules and ions into virtually every cell type.”
- ^ Boyd, C A R. “Facts, fantasies and fun in epithelial physiology”. Experimental Physiology, Vol. 93, Issue 3, 2008, p. 304. “the insight from this time that remains in all current text books is the notion of Robert Crane published originally as an appendix to a symposium paper published in 1960 (Crane et al. 1960). The key point here was 'flux coupling', the cotransport of sodium and glucose in the apical membrane of the small intestinal epithelial cell. Half a century later this idea has turned into one of the most studied of all transporter proteins (SGLT1), the sodium–glucose cotransporter.”
By group SLC1–10
- (6) sodium- and chloride- dependent sodium:neurotransmitter symporters (SLC6A1, SLC6A2, SLC6A3, SLC6A4, SLC6A5, SLC6A6, SLC6A7, SLC6A8, SLC6A9, SLC6A10, SLC6A11, SLC6A12, SLC6A13, SLC6A14, SLC6A15, SLC6A16, SLC6A17, SLC6A18, SLC6A19, SLC6A20)
- (7) cationic amino-acid transporter/glycoprotein-associated (SLC7A1, SLC7A2, SLC7A3, SLC7A4) glycoprotein-associated/light or catalytic subunits of heterodimeric amino-acid transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A9, SLC7A10, SLC7A11, SLC7A13, SLC7A14)
- (8) Na+/Ca2+ exchanger (SLC8A1, SLC8A2, SLC8A3)
- (9) Na+/H+ exchanger (SLC9A1, SLC9A2, SLC9A3, SLC9A4, SLC9A5, SLC9A6, SLC9A7, SLC9A8, SLC9A9, SLC9A10, SLC9A11)
- (12) electroneutral cation-Cl cotransporter (SLC12A1, SLC12A1, SLC12A2, SLC12A3, SLC12A4, SLC12A5, SLC12A6, SLC12A7, SLC12A8, SLC12A9)
- (15) proton oligopeptide cotransporter (SLC15A1, SLC15A2, SLC15A3, SLC15A4)
- (16) monocarboxylate transporter (SLC16A1, SLC16A2, SLC16A3, SLC16A4, SLC16A5, SLC16A6, SLC16A7, SLC16A8, SLC16A9, SLC16A10, SLC16A11, SLC16A12, SLC16A13, SLC16A14)
- (17) vesicular glutamate transporter (SLC17A1, SLC17A2, SLC17A3, SLC17A4, SLC17A5, SLC17A6, SLC17A7, SLC17A8, SLC17A9)
- (21) organic anion transporting (SLCO1A2, SLCO1B1, SLCO1B3, SLCO1B4, SLCO1C1) (SLCO2A1, SLCO2B1) (SLCO3A1) (SLCO4A1, SLCO4C1) (SLCO5A1) (SLCO6A1)
- (22) organic cation/anion/zwitterion transporter (SLC22A1, SLC22A2, SLC22A3, SLC22A4, SLC22A5, SLC22A6, SLC22A7, SLC22A8, SLC22A9, SLC22A10, SLC22A11, SLC22A12, SLC22A13, SLC22A14, SLC22A15, SLC22A16, SLC22A17, SLC22A18, SLC22A19, SLC22A20)
- (24) Na+/(Ca2+-K+) exchanger (SLC24A1, SLC24A2, SLC24A3, SLC24A4, SLC24A5, SLC24A6)
- (25) mitochondrial carrier (SLC25A1, SLC25A2, SLC25A3, SLC25A4, SLC25A5, SLC25A6, SLC25A7, SLC25A8, SLC25A9, SLC25A10, SLC25A11, SLC25A12, SLC25A13, SLC25A14, SLC25A15, SLC25A16, SLC25A17, SLC25A18, SLC25A19, SLC25A20, SLC25A21, SLC25A22, SLC25A23, SLC25A24, SLC25A25, SLC25A26, SLC25A27, SLC25A28, SLC25A29, SLC25A30, SLC25A31, SLC25A32, SLC25A33, SLC25A34, SLC25A35, SLC25A36, SLC25A37, SLC25A38, SLC25A39, SLC25A40, SLC25A41, SLC25A42, SLC25A43, SLC25A44, SLC25A45, SLC25A46)
- (26) multifunctional anion exchanger (SLC26A1, SLC26A2, SLC26A3, SLC26A4, SLC26A5, SLC26A6, SLC26A7, SLC26A8, SLC26A9, SLC26A10, SLC26A11)
- (32) vesicular inhibitory amino-acid transporter (SLC32A1)
- (33) Acetyl-CoA transporter (SLC33A1)
- (35) nucleoside-sugar transporter (SLC35A1, SLC35A2, SLC35A3, SLC35A4, SLC35A5) (SLC35B1, SLC35B2, SLC35B3, SLC35B4) (SLC35C1, SLC35C2) (SLC35D1, SLC35D2, SLC35D3) (SLC35E1, SLC35E2, SLC35E3, SLC35E4)
- (36) proton-coupled amino-acid transporter (SLC36A1, SLC36A2, SLC36A3, SLC36A4)36A2 ·
- (37) sugar-phosphate/phosphate exchanger (SLC37A1, SLC37A2, SLC37A3, SLC37A4)
- (38) System A & N, sodium-coupled neutral amino-acid transporter (SLC38A1, SLC38A2, SLC38A3, SLC38A4, SLC38A5, SLC38A6, SLC38A10)
- (39) metal ion transporter (SLC39A1, SLC39A2, SLC39A3, SLC39A4, SLC39A5, SLC39A6, SLC39A7, SLC39A8, SLC39A9, SLC39A10, SLC39A11, SLC39A12, SLC39A13, SLC39A14)
- (40) basolateral iron transporter (SLC40A1)
- (41) MgtE-like magnesium transporter (SLC41A1, SLC41A2, SLC41A3)
- (43) Na+-independent, system-L like amino-acid transporter (SLC43A1, SLC43A2, SLC43A3)
- (45) Putative sugar transporter (SLC45A1, SLC45A2, SLC54A3, SLC45A4)
- (46) Folate transporter (SLC46A1, SLC46A2)
- (48) Heme transporter
SLCO1–4 Ion pumps
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